Q570Y9 · DPTOR_MOUSE
- ProteinDEP domain-containing mTOR-interacting protein
- GeneDeptor
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids409 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score4/5
Function
function
Negative regulator of the mTORC1 and mTORC2 complexes: inhibits the protein kinase activity of MTOR, thereby inactivating both complexes. DEPTOR inhibits mTORC1 and mTORC2 to induce autophagy. In contrast to AKT1S1/PRAS40, only partially inhibits mTORC1 activity.
Activity regulation
Inhibited upon phosphatidic acid-binding: phosphatidic acid produced upon mitogenic stimulation promotes DEPTOR dissociatiom from the mTORC1 and mTORC2 complexes, leading to their activation. Specifically binds unsaturated phosphatidic acid, such as 16:0-18:1, 18:0-18:1 and di-18:1. Inhibited when nutrients are present via a feedback loop: phosphorylation by MTOR promotes DEPTOR ubiquitination and degradation.
GO annotations
all annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Aspect | Term | |
---|---|---|
Cellular Component | lysosomal membrane | |
Molecular Function | phosphatidic acid binding | |
Molecular Function | protein kinase inhibitor activity | |
Molecular Function | protein serine/threonine kinase inhibitor activity | |
Biological Process | intracellular signal transduction | |
Biological Process | negative regulation of cell size | |
Biological Process | negative regulation of TORC1 signaling | |
Biological Process | negative regulation of TORC2 signaling | |
Biological Process | positive regulation of autophagy | |
Biological Process | regulation of extrinsic apoptotic signaling pathway |
Keywords
- Ligand
Names & Taxonomy
Protein names
- Recommended nameDEP domain-containing mTOR-interacting protein
- Alternative names
Gene names
Organism names
- Organism
- Strain
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Glires > Rodentia > Myomorpha > Muroidea > Muridae > Murinae > Mus > Mus
Accessions
- Primary accessionQ570Y9
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
UniProt Annotation
GO Annotation
Note: Localizes to the lysosomal membrane when associated with the mTORC1 and mTORC2 complexes.
Keywords
- Cellular component
PTM/Processing
Features
Showing features for modified residue, chain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Modified residue | 1 | N-acetylmethionine | ||||
Sequence: M | ||||||
Chain | PRO_0000284785 | 1-409 | DEP domain-containing mTOR-interacting protein | |||
Sequence: MEEGSSGGSGSSDSNAGGSGGVQQRELERMAEVLVTGEQLRLRLHEEKVIKDRRHHLKTYPNCFVAKELIDWLIEHKEASDRETAIKLMQKLADRGIIHHVCDEHKEFKDVKLFYRFRKDDGTFALDSEVKAFMRGQRLYEKLMSPETTLLQPREEEGVKYERTFMASEFLDWLVQEGEATTRKEAEQLCHRLMDHGIIQHVSNKHPFVDSNLLYQFRMNFRRRRRLMELLNETSPSSQETHDSPFCLRKQSHDSRKSTSFMSVSPSKEIKIVSAVRRSSMSSCGSSGYFSSSPTLSSSPPVLCNPKSVLKRPVTSEELLTPGAPYARKTFTIVGDAVGWGFVVRGSKPCHIQAVDPSGPAAAAGMKVCQFVVSVNGLNVLNVDYRTVSNLILTGPRTIVMEVMEELDC | ||||||
Modified residue | 235 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 241 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 244 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 258 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 259 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 263 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 265 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 280 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 282 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 283 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 286 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 287 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 289 | Phosphotyrosine | ||||
Sequence: Y | ||||||
Modified residue | 291 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 293 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 295 | Phosphothreonine | ||||
Sequence: T | ||||||
Modified residue | 297 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 298 | Phosphoserine | ||||
Sequence: S | ||||||
Modified residue | 299 | Phosphoserine | ||||
Sequence: S |
Post-translational modification
Phosphorylation weakens interaction with MTOR within mTORC1 and mTORC2 (By similarity).
Phosphorylated at Ser-286, Ser-287 and Ser-291 in response to mitogenic stimulation by MTOR: DEPTOR is either directly phosphorylated by MTOR or indirectly via proteins kinases that are activated by MTOR, such as CK1/CSNK1A1 (By similarity).
Phosphorylation at Ser-286, Ser-287 and Ser-291 promotes ubiquitination by the SCF(BTRC) complex, followed by degradation (By similarity).
Phosphorylation at Ser-235 by MAPK3/ERK1 promotes deubiquitination by USP7, enhancing its stability (By similarity).
Phosphorylation at Tyr-291 by SYK impairs its interaction with MTOR, promoting mTORC1 and mTORC2 signaling (By similarity).
Phosphorylated at Ser-286, Ser-287 and Ser-291 in response to mitogenic stimulation by MTOR: DEPTOR is either directly phosphorylated by MTOR or indirectly via proteins kinases that are activated by MTOR, such as CK1/CSNK1A1 (By similarity).
Phosphorylation at Ser-286, Ser-287 and Ser-291 promotes ubiquitination by the SCF(BTRC) complex, followed by degradation (By similarity).
Phosphorylation at Ser-235 by MAPK3/ERK1 promotes deubiquitination by USP7, enhancing its stability (By similarity).
Phosphorylation at Tyr-291 by SYK impairs its interaction with MTOR, promoting mTORC1 and mTORC2 signaling (By similarity).
Ubiquitinated; leading to proteasomal degradation (By similarity).
Ubiquitination by the SCF(BTRC) and SCF(FBXW11) complexes following phosphorylation at Ser-286, Ser-287 and Ser-291 by MTOR, leads to its degradation by the proteasome (By similarity).
Deubiquitinated by OTUB1 in response to amino acid via a non-canonical mechanism, leading to DEPTOR stability (By similarity).
Deubiquitinated by USP7 following phosphorylation at Ser-235, promoting its stability (By similarity).
Ubiquitination by the SCF(BTRC) and SCF(FBXW11) complexes following phosphorylation at Ser-286, Ser-287 and Ser-291 by MTOR, leads to its degradation by the proteasome (By similarity).
Deubiquitinated by OTUB1 in response to amino acid via a non-canonical mechanism, leading to DEPTOR stability (By similarity).
Deubiquitinated by USP7 following phosphorylation at Ser-235, promoting its stability (By similarity).
Keywords
- PTM
Proteomic databases
PTM databases
Expression
Developmental stage
At postnatal day 1 (P1), in cartilage growth plate, primarily expressed in resting and proliferating chondrocytes. This expression pattern is maintained at least until P21 (at protein level).
Gene expression databases
Interaction
Subunit
Associated component of the mechanistic target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8 and RPTOR. Associated component of the mechanistic target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PROTOR1, RICTOR, MAPKAP1 and DEPTOR. Interacts (via PDZ domain) with MTOR; interacts with MTOR within both mTORC1 and mTORC2. Interacts (via PDZ domain) with MINAR1 (via N-terminus). Interacts with SIK3.
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for compositional bias, region, domain, motif.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MEEGSSGGSGSSDSNAGGSGG | ||||||
Region | 1-23 | Disordered | ||||
Sequence: MEEGSSGGSGSSDSNAGGSGGVQ | ||||||
Domain | 36-119 | DEP 1 | ||||
Sequence: TGEQLRLRLHEEKVIKDRRHHLKTYPNCFVAKELIDWLIEHKEASDRETAIKLMQKLADRGIIHHVCDEHKEFKDVKLFYRFRK | ||||||
Domain | 146-219 | DEP 2 | ||||
Sequence: PETTLLQPREEEGVKYERTFMASEFLDWLVQEGEATTRKEAEQLCHRLMDHGIIQHVSNKHPFVDSNLLYQFRM | ||||||
Motif | 217-235 | DDEX motif | ||||
Sequence: FRMNFRRRRRLMELLNETS | ||||||
Motif | 286-291 | BetaTrCP degron motif | ||||
Sequence: SSGYFS | ||||||
Domain | 330-407 | PDZ | ||||
Sequence: TFTIVGDAVGWGFVVRGSKPCHIQAVDPSGPAAAAGMKVCQFVVSVNGLNVLNVDYRTVSNLILTGPRTIVMEVMEEL |
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
This entry describes 3 isoforms produced by Alternative splicing.
Q570Y9-1
This isoform has been chosen as the canonical sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
- Name1
- Length409
- Mass (Da)46,120
- Last updated2007-04-17 v2
- Checksum072062418DADDF8E
Q570Y9-2
- Name2
- Differences from canonical
- 1-40: MEEGSSGGSGSSDSNAGGSGGVQQRELERMAEVLVTGEQL → MKQAFLVVLRHSISEDRLPPLSVITSGC
Q570Y9-3
- Name3
- Differences from canonical
- 368-409: VCQFVVSVNGLNVLNVDYRTVSNLILTGPRTIVMEVMEELDC → DTGTESRKIVTSRLAWATWQDLMGGKVGGDAIPI
Computationally mapped potential isoform sequences
There are 2 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
A0A2I3BRE1 | A0A2I3BRE1_MOUSE | Deptor | 100 | ||
B2ZRS5 | B2ZRS5_MOUSE | Deptor | 401 |
Sequence caution
Features
Showing features for compositional bias, alternative sequence, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Compositional bias | 1-21 | Polar residues | ||||
Sequence: MEEGSSGGSGSSDSNAGGSGG | ||||||
Alternative sequence | VSP_024648 | 1-40 | in isoform 2 | |||
Sequence: MEEGSSGGSGSSDSNAGGSGGVQQRELERMAEVLVTGEQL → MKQAFLVVLRHSISEDRLPPLSVITSGC | ||||||
Sequence conflict | 11 | in Ref. 2; BAE26298 | ||||
Sequence: S → G | ||||||
Sequence conflict | 125 | in Ref. 2; BAE26298 | ||||
Sequence: A → P | ||||||
Sequence conflict | 128 | in Ref. 2; BAE26298 | ||||
Sequence: S → N | ||||||
Sequence conflict | 149 | in Ref. 2; BAE26298 | ||||
Sequence: T → I | ||||||
Alternative sequence | VSP_024649 | 368-409 | in isoform 3 | |||
Sequence: VCQFVVSVNGLNVLNVDYRTVSNLILTGPRTIVMEVMEELDC → DTGTESRKIVTSRLAWATWQDLMGGKVGGDAIPI |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
AK220300 EMBL· GenBank· DDBJ | BAD90225.1 EMBL· GenBank· DDBJ | mRNA | Different initiation | |
AK139888 EMBL· GenBank· DDBJ | BAE24172.1 EMBL· GenBank· DDBJ | mRNA | ||
AK145208 EMBL· GenBank· DDBJ | BAE26298.1 EMBL· GenBank· DDBJ | mRNA |